1ENH

STRUCTURAL STUDIES OF THE ENGRAILED HOMEODOMAIN

Summary for 1ENH

• Entry DOI: 10.2210/pdb1enh/pdb
• Descriptor: ENGRAILED HOMEODOMAIN (2 entities in total)
• Functional Keywords: dna-binding protein, dna binding protein
• Biological source: Drosophila melanogaster (fruit fly)
• Cellular location: Nucleus: P02836
• Total number of polymer chains: 1
• Total formula weight: 6619.54

Authors

Clarke, N.D.,Kissinger, C.R.,Desjarlais, J.,Gilliland, G.L.,Pabo, C.O. (deposition date: 1994-05-20, release date: 1994-08-31, Last modification date: 2024-02-07)

Primary citation

Clarke, N.D.,Kissinger, C.R.,Desjarlais, J.,Gilliland, G.L.,Pabo, C.O.
Structural studies of the engrailed homeodomain.
Protein Sci., 3:1779-1787, 1994

PubMed Abstract: The structure of the Drosophila engrailed homeodomain has been solved by molecular replacement and refined to an R-factor of 19.7% at a resolution of 2.1 A. This structure offers a high-resolution view of an important family of DNA-binding proteins and allows comparison to the structure of the same protein bound to DNA. The most significant difference between the current structure and that of the 2.8-A engrailed-DNA complex is the close packing of an extended strand against the rest of the protein in the unbound protein. Structural features of the protein not previously noted include a "herringbone" packing of 4 aromatic residues in the core of the protein and an extensive network of salt bridges that covers much of the helix 1-helix 2 surface. Other features that may play a role in stabilizing the native state include the interaction of buried carbonyl oxygen atoms with the edge of Phe 49 and a bias toward statistically preferred side-chain dihedral angles. There is substantial disorder at both ends of the 61 amino acid protein. A 51-amino acid variant of engrailed (residues 6-56) was synthesized and shown by CD and thermal denaturation studies to be structurally and thermodynamically similar to the full-length domain.

PubMed: 7849596

Experimental method

X-RAY DIFFRACTION (2.1 Å)